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Trimethylamine-N-oxide-induced folding of alpha-synucleinстатья
Статья опубликована в высокорейтинговом журнале
Статья опубликована в журнале из списка Web of Science и/или Scopus- Авторы: Uversky Vladimir N., Li Jie, Fink Anthony L.
- Журнал: FEBS Letters
- Том: 509
- Номер: 1
- Год издания: 2001
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 31
- Последняя страница: 35
- DOI: 10.1016/s0014-5793(01)03121-0
- Аннотация: The effect of the natural osmolyte trimethylamine-N-oxide (TMAO) on the structural properties and fibril formation of the natively unfolded protein human alpha-synuclein was studied using several physico-chemical methods. TMAO induced folding of alpha-synuclein: at moderate concentrations, a partially folded intermediate with enhanced propensity for fibrillation accumulated; at higher concentrations, alpha-synuclein was tightly folded and underwent self-association to form oligomers. The latter conformation was significantly helical and probably represents the physiologically folded form of the protein.
- Добавил в систему: Уверский Владимир Николаевич